B. Kokke

The chaperone-like activity of a small heat shock protein is lost after sulfoxidation of conserved methionines in a surface-exposed amphipathic alpha-helix.

F. Tjerneld, S. Linse, N. Gustavsson, 2001, Biochimica et biophysica acta.

A platform for the generation of site-specific antibody-drug conjugates that allows for selective reduction of engineered cysteines.

R. Ubink, P. Beusker, M. Blomenröhr, 2020, Bioconjugate chemistry.

Organogel formation and molecular imprinting by functionalized gluconamides and their metal complexes

M. C. Feiters, Rudi J. H. Hafkamp, R. Nolte, 1997 .

Substitution of conserved methionines by leucines in chloroplast small heat shock protein results in loss of redox‐response but retained chaperone‐like activity

N. Gustavsson, W. Boelens, C. Sundby, 2001, Protein science : a publication of the Protein Society.

A peptide methionine sulfoxide reductase highly expressed in photosynthetic tissue in Arabidopsis thaliana can protect the chaperone-like activity of a chloroplast-localized small heat shock protein.

D. Murphy, N. Gustavsson, W. Boelens, 2002, The Plant journal : for cell and molecular biology.

Characterization of highly concentrated antibody solution - A toolbox for the description of protein long-term solution stability

Jürgen Hubbuch, Marie-Therese Schermeyer, M. Eppink, 2017, mAbs.

The rodent αA-crystallin gene: mutagenesis of a non-consensus 5′-splice site to study alternative splicing in vivo

W. D. de Jong, R. Smulders, B. Kokke, 1998, Molecular Biology Reports.

Caenorhabditis elegans small heat‐shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone‐like activity

W. D. de Jong, W. Boelens, M. Leroux, 1998, FEBS letters.